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Bugs, Fish Poison, Insecticide, Legumes, Salicaceae
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Ryania speciosa, Ryanodine and Ryanoids

Ryania speciosa is a species of plant in the family Salicaceae. The species is significant partly because the ryanoid insecticides are derived from, and have the same mode of action as the alkaloid ryanodine, which was originally extracted from this South American plant, which is also used as a piscicide (fish poison). M. Vahl, 1797 In: Eclog. Am. 1: 51, t. 9 (1796) [1797] The Plant list Roskov Y.; Kunze T.; Orrell T.; Abucay L.; Paglinawan L.; Culham A.; Bailly N.; Kirk P.; Bourgoin T.; Baillargeon G.; Decock W.; De Wever A. (2014). Didžiulis V. (ed.). “Species 2000 & ITIS Catalogue of Life: 2014 Annual Checklist”. Species 2000: Reading, UK. Retrieved 26 May 2014. World Plants: Synonymic Checklists of the Vascular Plants of the World USDA Phytochemistry

Varieties

The Catalogue of Life lists these varieties:

External links

  •  Media related to Salicaceae at Wikimedia Commons
  •  Data related to Ryania at Wikispecies

Ryanodine is a poisonous diterpenoid found in the South American plant Ryania speciosa (Salicaceae). It was originally used as an insecticide.

The compound has extremely high affinity to the open-form ryanodine receptor, a group of calcium channels found in skeletal muscle, smooth muscle, and heart muscle cells. It binds with such high affinity to the receptor that it was used as a label for the first purification of that class of ion channels and gave its name to it. Santulli, Gaetano; Marks, Andrew (2015). “Essential Roles of Intracellular Calcium Release Channels in Muscle, Brain, Metabolism, and Aging”. Current Molecular Pharmacology. 8 (2): 206–222. doi:10.2174/1874467208666150507105105. ISSN 1874-4672. PMID 25966694.

At nanomolar concentrations, ryanodine locks the receptor in a half-open state, whereas it fully closes them at micromolar concentration. The effect of the nanomolar-level binding is that ryanodine causes release of calcium from calcium stores as the sarcoplasmic reticulum in the cytoplasm, leading to massive muscle contractions. The effect of micromolar-level binding is paralysis. This is true for both mammals and insects. Van Petegem, F (2012). “Ryanodine receptors: structure and function”. The Journal of Biological Chemistry. 287 (38): 31624–32. doi:10.1074/jbc.r112.349068. PMC 3442496. PMID 22822064.

Ryanoids

Ryanoids are a class of insecticides which share the same mechanism of action as the alkaloid ryanodine. Ryanodine is a naturally occurring insecticide isolated from Ryania speciosa.

Ryanoids include natural chemicals which are closely related to ryanodine, such as ryanodol and 9,21-didehydroryanodol, and also chemically distinct synthetic compounds such as chlorantraniliprole (Rynaxypyr), flubendiamide, cyantraniliprole, cyclaniliprole, and tetraniliprole, which are called diamide insecticides. Ryanoids exert their insecticidal effect by interacting with ryanodine receptors, a type of calcium channel. This causes loss of muscle function[3] leading to paralysis and death. Usherwood, P.N.R.; Vais, H. (1995). “Towards the development of ryanoid insecticides with low mammalian toxicity”. Toxicology Letters. 82–83: 247–54. doi:10.1016/0378-4274(95)03558-3. PMID 8597061. Teixeira, Luís A; Andaloro, John T (2013). “Diamide insecticides: Global efforts to address insect resistance stewardship challenges”. Pesticide Biochemistry and Physiology. 106 (3): 76–78. doi:10.1016/j.pestbp.2013.01.010. IRAC International MoA Working Group (March 2020). “IRAC Mode of Action Classification Scheme Version 9.4”. Insecticide Resistance Action Committee.

Further reading

  1. Essential Roles of Intracellular Calcium Release Channels in Muscle, Brain, Metabolism, and Aging Current Molecular Pharmacology vol.8, 2015, pages=206–222, ISSN 1874-4672
  2. Bertil Hille, Ionic Channels of Excitable Membranes, 2nd edition, Sinauer Associates, Sunderland, MA, 01375, ISBN 0-87893-323-9

Ryanodine receptors

Ryanodine receptors (RyR for short) form a class of intracellular calcium channels in various forms of excitable animal tissue like muscles and neurons.[1] There are three major isoforms of the ryanodine receptor, which are found in different tissues and participate in different signaling pathways involving calcium release from intracellular organelles. The RYR2 ryanodine receptor isoform is the major cellular mediator of calcium-induced calcium release (CICR) in animal cells.

Ryanodine receptors (RyR for short) form a class of intracellular calcium channels in various forms of excitable animal tissue like muscles and neurons.[1] There are three major isoforms of the ryanodine receptor, which are found in different tissues and participate in different signaling pathways involving calcium release from intracellular organelles. The RYR2 ryanodine receptor isoform is the major cellular mediator of calcium-induced calcium release (CICR) in animal cells.

Etymology

The ryanodine receptors are named after the plant alkaloid ryanodine which shows a high affinity to them.

Isoforms

There are multiple isoforms of ryanodine receptors:

  • RyR1 is primarily expressed in skeletal muscle
  • RyR2 is primarily expressed in myocardium (heart muscle)
  • RyR3 is expressed more widely, but especially in the brain.[2]
  • Non-mammalian vertebrates typically express two RyR isoforms, referred to as RyR-alpha and RyR-beta.
  • Many invertebrates, including the model organisms Drosophila melanogaster (fruitfly) and Caenorhabditis elegans, only have a single isoform. In non-metazoan species, calcium-release channels with sequence homology to RyRs can be found, but they are shorter than the mammalian ones and may be closer to IP3 Receptors.
ryanodine receptor 1 (skeletal)
Identifiers
SymbolRYR1
Alt. symbolsMHS, MHS1, CCO
NCBI gene6261
HGNC10483
OMIM180901
RefSeqNM_000540
UniProtP21817
Other data
LocusChr. 19 q13.1
show

Ryanodine receptor 1 (RYR-1) also known as skeletal muscle calcium release channel or skeletal muscle-type ryanodine receptor is one of a class of ryanodine receptors and a protein found primarily in skeletal muscle. In humans, it is encoded by the RYR1gene. Fujii J, Otsu K, Zorzato F, de Leon S, Khanna VK, Weiler JE, O’Brien PJ, MacLennan DH (July 1991). “Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia”. Science. 253 (5018): 448–51. Bibcode:1991Sci…253..448F. doi:10.1126/science.1862346. PMID 1862346. Wu S, Ibarra MC, Malicdan MC, Murayama K, Ichihara Y, Kikuchi H, Nonaka I, Noguchi S, Hayashi YK, Nishino I (June 2006). “Central core disease is due to RYR1 mutations in more than 90% of patients”. Brain. 129 (Pt 6): 1470–80. doi:10.1093/brain/awl077. PMID 16621918.

Function

RYR1 functions as a calcium release channel in the sarcoplasmic reticulum, as well as a connection between the sarcoplasmic reticulum and the transverse tubule. RYR1 is associated with the dihydropyridine receptor (L-type calcium channels) within the sarcolemma of the T-tubule, which opens in response to depolarization, and thus effectively means that the RYR1 channel opens in response to depolarization of the cell. “Entrez Gene: RYR1 ryanodine receptor 1 (skeletal)”

RYR1 plays a signaling role during embryonic skeletal myogenesis. A correlation exists between RYR1-mediated Ca2+ signaling and the expression of multiple molecules involved in key myogenic signaling pathways. Of these, more than 10 differentially expressed genes belong to the Wnt family which are essential for differentiation. This coincides with the observation that without RYR1 present, muscle cells appear in smaller groups, are underdeveloped, and lack organization. Fiber type composition is also affected, with less type 1 muscle fibers when there are decreased amounts of RYR1. These findings demonstrate RYR1 has a non-contractile role during muscle development. Filipova D, Walter AM, Gaspar JA, Brunn A, Linde NF, Ardestani MA, Deckert M, Hescheler J, Pfitzer G, Sachinidis A, Papadopoulos S (April 2016). “Corrigendum: Gene profiling of embryonic skeletal muscle lacking type I ryanodine receptor Ca(2+) release channel”. Scientific Reports. 6: 24450. Bibcode:2016NatSR…624450F. doi:10.1038/srep24450. PMC 4840354. PMID 27102063. Willemse H, Theodoratos A, Smith PN, Dulhunty AF (February 2016). “Unexpected dependence of RyR1 splice variant expression in human lower limb muscles on fiber-type composition”. Pflügers Archiv. 468 (2): 269–78. doi:10.1007/s00424-015-1738-9. PMID 26438192. S2CID 5894066.

RYR1 is mechanically linked to neuromuscular junctions for the calcium release-calcium induced biological process. While nerve-derived signals are required for acetylcholine receptor cluster distribution, there is evidence to suggest RYR1 activity is an important mediator in the formation and patterning of these receptors during embryological development. The signals from the nerve and RYR1 activity appear to counterbalance each other. When RYR1 is eliminated, the acetylcholine receptor clusters appear in an abnormally narrow pattern, yet without signals from the nerve, the clusters are scattered and broad. Although their direct role is still unknown, RYR1 is required for proper distribution of acetylcholine receptor clusters. Hanson MG, Niswander LA (December 2014). “An explant muscle model to examine the refinement of the synaptic landscape”. Journal of Neuroscience Methods. 238: 95–104. doi:10.1016/j.jneumeth.2014.09.013. PMC 4252626. PMID 25251554.

Clinical significance

Mutations in the RYR1 gene are associated with malignant hyperthermia susceptibility, central core disease, minicore myopathy with external ophthalmoplegia and samaritan myopathy, a benign congenital myopathy. Alternatively spliced transcripts encoding different isoforms have been demonstrated. Dantrolene may be the only known drug that is effective during cases of malignant hyperthermia.[citation needed] “Entrez Gene: RYR1 ryanodine receptor 1 (skeletal)“ Böhm J, Leshinsky-Silver E, Vassilopoulos S, Le Gras S, Lerman-Sagie T, Ginzberg M, Jost B, Lev D, Laporte J (October 2012). “Samaritan myopathy, an ultimately benign congenital myopathy, is caused by a RYR1 mutation”. Acta Neuropathologica. 124 (4): 575–81. doi:10.1007/s00401-012-1007-3. PMID 22752422. S2CID 9014320.

Interactions

RYR1 has been shown to interact with:

Further reading

  • Treves S, Anderson AA, Ducreux S, Divet A, Bleunven C, Grasso C, Paesante S, Zorzato F (October 2005). “Ryanodine receptor 1 mutations, dysregulation of calcium homeostasis and neuromuscular disorders”. Neuromuscular Disorders. 15 (9–10): 577–87. doi:10.1016/j.nmd.2005.06.008. PMID 16084090. S2CID 31372661.

External links

ryanodine receptor 2 (cardiac)
Identifiers
SymbolRYR2
NCBI gene6262
HGNC10484
OMIM180902
RefSeqNM_001035
UniProtQ92736
Other data
LocusChr. 1 q42.1-q43

Ryanodine receptor 2 (RYR2) is one of a class of ryanodine receptors and a protein found primarily in cardiac muscle. In humans, it is encoded by the RYR2gene. In the process of cardiac calcium-induced calcium release, RYR2 is the major mediator for sarcoplasmic release of stored calcium ions. Otsu K, Willard HF, Khanna VK, Zorzato F, Green NM, MacLennan DH (August 1990). “Molecular cloning of cDNA encoding the Ca2+ release channel (ryanodine receptor) of rabbit cardiac muscle sarcoplasmic reticulum”. The Journal of Biological Chemistry. 265 (23): 13472–83. doi:10.1016/S0021-9258(18)77371-7. PMID 2380170. Otsu K, Fujii J, Periasamy M, Difilippantonio M, Uppender M, Ward DC, MacLennan DH (August 1993). “Chromosome mapping of five human cardiac and skeletal muscle sarcoplasmic reticulum protein genes”. Genomics. 17 (2): 507–9. doi:10.1006/geno.1993.1357. PMID 8406504. Tiso N, Stephan DA, Nava A, Bagattin A, Devaney JM, Stanchi F, et al. (February 2001). “Identification of mutations in the cardiac ryanodine receptor gene in families affected with arrhythmogenic right ventricular cardiomyopathy type 2 (ARVD2)”. Human Molecular Genetics. 10 (3): 189–94. doi:10.1093/hmg/10.3.189. PMID 11159936.

Structure

The channel is composed of RYR2 homotetramers and FK506-binding proteins found in a 1:4 stoichiometric ratio. Calcium channel function is affected by the specific type of FK506 isomer interacting with the RYR2 protein, due to binding differences and other factors. Guo T, Cornea RL, Huke S, Camors E, Yang Y, Picht E, et al. (June 2010). “Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized cardiac myocytes and effects on Ca sparks”. Circulation Research. 106 (11): 1743–52. doi:10.1161/CIRCRESAHA.110.219816. PMC 2895429. PMID 20431056.

Function

The RYR2 protein functions as the major component of a calcium channel located in the sarcoplasmic reticulum that supplies ions to the cardiac muscle during systole. To enable cardiac muscle contraction, calcium influx through voltage-gated L-type calcium channels in the plasma membrane allows calcium ions to bind to RYR2 located on the sarcoplasmic reticulum. This binding causes the release of calcium through RYR2 from the sarcoplasmic reticulum into the cytosol, where it binds to the C domain of troponin, which shifts tropomyosin and allows the myosin ATPase to bind to actin, enabling cardiac muscle contraction. RYR2 channels are associated with many cellular functions, including mitochondrial metabolism, gene expression and cell survival, in addition to their role in cardiomyocyte contraction. “Q92736 – RYR2_HUMAN“. Bround MJ, Wambolt R, Luciani DS, Kulpa JE, Rodrigues B, Brownsey RW, et al. (June 2013). “Cardiomyocyte ATP production, metabolic flexibility, and survival require calcium flux through cardiac ryanodine receptors in vivo”. The Journal of Biological Chemistry. 288 (26): 18975–86. doi:10.1074/jbc.M112.427062. PMC 3696672. PMID 23678000.

Clinical significance

Deleterious mutations of the ryanodine receptor family, and especially the RYR2 receptor, lead to a constellation of pathologies leading to both acute and chronic heart failure collectively known as “Ryanopathies.” Mutations in the RYR2 gene are associated with catecholaminergic polymorphic ventricular tachycardia and arrhythmogenic right ventricular dysplasia. Belevych AE, Radwański PB, Carnes CA, Györke S (May 2013). “‘Ryanopathy’: causes and manifestations of RyR2 dysfunction in heart failure”. Cardiovascular Research. 98 (2): 240–7. doi:10.1093/cvr/cvt024. PMC 3633158. PMID 23408344. “Entrez Gene: RYR2 ryanodine receptor 2 (cardiac)”.

Recently, sudden cardiac death in several young individuals in the Amish community (four of which were from the same family) was traced to homozygous duplication of a mutant RyR2 gene. Normal (wild type) RyR2 functions primarily in the myocardium (heart muscle). Mice with genetically reduced RYR2 exhibit a lower basal heart rate and fatal arrhythmias. Tester DJ, Bombei HM, Fitzgerald KK, Giudicessi JR, Pitel BA, Thorland EC, et al. (January 2020). “Identification of a Novel Homozygous Multi-Exon Duplication in RYR2 Among Children With Exertion-Related Unexplained Sudden Deaths in the Amish Community”. JAMA Cardiology. 5 (3): 13–18. doi:10.1001/jamacardio.2019.5400. PMC 6990654. PMID 31913406. Bround MJ, Asghari P, Wambolt RB, Bohunek L, Smits C, Philit M, et al. (December 2012). “Cardiac ryanodine receptors control heart rate and rhythmicity in adult mice”. Cardiovascular Research. 96 (3): 372–80. doi:10.1093/cvr/cvs260. PMC 3500041. PMID 22869620

Interactions

Ryanodine receptor 2 has been shown to interact with:

ryanodine receptor 3
Identifiers
SymbolRYR3
NCBI gene6263
HGNC10485
OMIM180903
RefSeqNM_001036
UniProtQ15413
Other data
LocusChr. 15 q14-q15

Ryanodine receptor 3 is one of a class of ryanodine receptors and a protein that in humans is encoded by the RYR3gene. The protein encoded by this gene is both a calcium channel and a receptor for the plant alkaloidryanodine. RYR3 and RYR1 control the resting calcium ion concentration in skeletal muscle. Sorrentino V, Giannini G, Malzac P, Mattei MG (Feb 1994). “Localization of a novel ryanodine receptor gene (RYR3) to human chromosome 15q14-q15 by in situ hybridization”. Genomics. 18 (1): 163–5. doi:10.1006/geno.1993.1446. PMID 8276408. Perez CF, López JR, Allen PD (March 2005). “Expression levels of RyR1 and RyR3 control resting free Ca2+ in skeletal muscle”. Am. J. Physiol., Cell Physiol. 288 (3): C640–9. doi:10.1152/ajpcell.00407.2004. PMID 15548569. S2CID 30888541.

Further reading

External links

Physiology

Ryanodine receptors mediate the release of calcium ions from the sarcoplasmic reticulum and endoplasmic reticulum, an essential step in muscle contraction.[1] In skeletal muscle, activation of ryanodine receptors occurs via a physical coupling to the dihydropyridine receptor (a voltage-dependent, L-type calcium channel), whereas, in cardiac muscle, the primary mechanism of activation is calcium-induced calcium release, which causes calcium outflow from the sarcoplasmic reticulum.[3]

It has been shown that calcium release from a number of ryanodine receptors in a ryanodine receptor cluster results in a spatiotemporally restricted rise in cytosolic calcium that can be visualised as a calcium spark.[4] Ryanodine receptors are very close to mitochondria and calcium release from RyR has been shown to regulate ATP production in heart and pancreas cells.[5][6][7]

Ryanodine receptors are similar to the inositol trisphosphate (IP3) receptor, and stimulated to transport Ca2+ into the cytosol by recognizing Ca2+ on its cytosolic side, thus establishing a positive feedback mechanism; a small amount of Ca2+ in the cytosol near the receptor will cause it to release even more Ca2+ (calcium-induced calcium release/CICR).[1] However, as the concentration of intracellular Ca2+ rises, this can trigger closing of RyR, preventing the total depletion of SR. This finding therefore indicates that a plot of opening probability for RyR as a function of Ca2+ concentration is a bell-curve.[8] Furthermore, RyR can sense the Ca2+ concentration inside the ER/SR and spontaneously open in a process known as store overload-induced calcium release (SOICR).[9]

RyRs are especially important in neurons and muscle cells. In heart and pancreas cells, another second messenger (cyclic ADP-ribose) takes part in the receptor activation.

The localized and time-limited activity of Ca2+ in the cytosol is also called a Ca2+ wave. The building of the wave is done by

Associated proteins

RyRs form docking platforms for a multitude of proteins and small molecule ligands.[1] The cardiac-specific isoform of the receptor (RyR2) is known to form a quaternary complex with luminal calsequestrin, junctin, and triadin.[10] Calsequestrin has multiple Ca2+ binding sites and binds Ca2+ ions with very low affinity so they can be easily released.

Pharmacology

  • Antagonists:[11]
  • Activators:[12]
    • Agonist: 4-chloro-m-cresol and suramin are direct agonists, i.e., direct activators.
    • Xanthines like caffeine and pentifylline activate it by potentiating sensitivity to native ligand Ca.
    • Physiological agonist: Cyclic ADP-ribose can act as a physiological gating agent. It has been suggested that it may act by making FKBP12.6 (12.6 kilodalton FK506 binding protein, as opposed to 12 kDa FKBP12 which binds to RyR1) which normally bind (and blocks) RyR2 channel tetramer in an average stoichiometry of 3.6, to fall off RyR2 (which is the predominant RyR in pancreatic beta cells, cardiomyocytes and smooth muscles).[13]

A variety of other molecules may interact with and regulate ryanodine receptor. For example: dimerized Homer physical tether linking inositol trisphosphate receptors (IP3R) and ryanodine receptors on the intracellular calcium stores with cell surface group 1 metabotropic glutamate receptors and the Alpha-1D adrenergic receptor[14]

Ryanodine

The plant alkaloid ryanodine, for which this receptor was named, has become an invaluable investigative tool. It can block the phasic release of calcium, but at low doses may not block the tonic cumulative calcium release. The binding of ryanodine to RyRs is use-dependent, that is the channels have to be in the activated state. At low (<10 micromolar, works even at nanomolar) concentrations, ryanodine binding locks the RyRs into a long-lived subconductance (half-open) state and eventually depletes the store, while higher (~100 micromolar) concentrations irreversibly inhibit channel-opening.

Caffeine

RyRs are activated by millimolar caffeine concentrations. High (greater than 5 mmol/L) caffeine concentrations cause a pronounced increase (from micromolar to picomolar) in the sensitivity of RyRs to Ca2+ in the presence of caffeine, such that basal Ca2+ concentrations become activatory. At low millimolar caffeine concentrations, the receptor opens in a quantal way, but has complicated behavior in terms of repeated use of caffeine or dependence on cytosolic or luminal calcium concentrations.

Role in disease

RyR1 mutations are associated with malignant hyperthermia and central core disease. RyR2 mutations play a role in stress-induced polymorphic ventricular tachycardia (a form of cardiac arrhythmia) and ARVD.[2] It has also been shown that levels of type RyR3 are greatly increased in PC12 cells overexpressing mutant human Presenilin 1, and in brain tissue in knockin mice that express mutant Presenilin 1 at normal levels,[15] and thus may play a role in the pathogenesis of neurodegenerative diseases, like Alzheimer’s disease.[16]

The presence of antibodies against ryanodine receptors in blood serum has also been associated with myasthenia gravis.[1]

Sudden cardiac death in several young individuals in the Amish community (four of which were from the same family) was traced to homozygous duplication of a mutant RyR2 (Ryanodine Receptor) gene.[17] Normal (wild type) ryanodine receptors are involved in CICR in heart and other muscles, and RyR2 functions primarily in the myocardium (heart muscle).

Structure

RyR1 cryo-EM structure revealed a large cytosolic assembly built on an extended α-solenoid scaffold connecting key regulatory domains to the pore. The RyR1 pore architecture shares the general structure of the six-transmembrane ion channel superfamily. A unique domain inserted between the second and third transmembrane helices interacts intimately with paired EF-hands originating from the α-solenoid scaffold, suggesting a mechanism for channel gating by Ca2+.[1][18]

See also

  • Ryanoid, a class of insecticide that act through ryanodine receptors

References

  1. ^ Jump up to:a b c d e f Santulli G, Marks AR (2015). “Essential Roles of Intracellular Calcium Release Channels in Muscle, Brain, Metabolism, and Aging”. Current Molecular Pharmacology. 8 (2): 206–22. doi:10.2174/1874467208666150507105105. PMID 25966694.
  2. ^ Jump up to:a b Zucchi R, Ronca-Testoni S (March 1997). “The sarcoplasmic reticulum Ca2+ channel/ryanodine receptor: modulation by endogenous effectors, drugs and disease states”. Pharmacological Reviews. 49 (1): 1–51. PMID 9085308.
  3. ^ Fabiato A (July 1983). “Calcium-induced release of calcium from the cardiac sarcoplasmic reticulum”. The American Journal of Physiology. 245 (1): C1-14. doi:10.1152/ajpcell.1983.245.1.C1. PMID 6346892.
  4. ^ Cheng H, Lederer WJ, Cannell MB (October 1993). “Calcium sparks: elementary events underlying excitation-contraction coupling in heart muscle”. Science. 262 (5134): 740–4. Bibcode:1993Sci…262..740C. doi:10.1126/science.8235594. PMID 8235594.
  5. ^ Bround MJ, Wambolt R, Luciani DS, Kulpa JE, Rodrigues B, Brownsey RW, et al. (June 2013). “Cardiomyocyte ATP production, metabolic flexibility, and survival require calcium flux through cardiac ryanodine receptors in vivo”. The Journal of Biological Chemistry. 288 (26): 18975–86. doi:10.1074/jbc.M112.427062. PMC 3696672. PMID 23678000.
  6. ^ Tsuboi T, da Silva Xavier G, Holz GG, Jouaville LS, Thomas AP, Rutter GA (January 2003). “Glucagon-like peptide-1 mobilizes intracellular Ca2+ and stimulates mitochondrial ATP synthesis in pancreatic MIN6 beta-cells”. The Biochemical Journal. 369 (Pt 2): 287–99. doi:10.1042/BJ20021288. PMC 1223096. PMID 12410638.
  7. ^ Dror V, Kalynyak TB, Bychkivska Y, Frey MH, Tee M, Jeffrey KD, et al. (April 2008). “Glucose and endoplasmic reticulum calcium channels regulate HIF-1beta via presenilin in pancreatic beta-cells”. The Journal of Biological Chemistry. 283 (15): 9909–16. doi:10.1074/jbc.M710601200. PMID 18174159.
  8. ^ Meissner G, Darling E, Eveleth J (January 1986). “Kinetics of rapid Ca2+ release by sarcoplasmic reticulum. Effects of Ca2+, Mg2+, and adenine nucleotides”. Biochemistry. 25 (1): 236–44. doi:10.1021/bi00349a033. PMID 3754147.
  9. ^ Van Petegem F (September 2012). “Ryanodine receptors: structure and function”. The Journal of Biological Chemistry. 287 (38): 31624–32. doi:10.1074/jbc.r112.349068. PMC 3442496. PMID 22822064.
  10. ^ Kranias E. “Dr. Evangelia Kranias Lab: Calsequestrin”. Retrieved 22 May 2014.
  11. ^ Vites AM, Pappano AJ (March 1994). “Distinct modes of inhibition by ruthenium red and ryanodine of calcium-induced calcium release in avian atrium”. The Journal of Pharmacology and Experimental Therapeutics. 268 (3): 1476–84. PMID 7511166.
  12. ^ Xu L, Tripathy A, Pasek DA, Meissner G (September 1998). “Potential for pharmacology of ryanodine receptor/calcium release channels”. Annals of the New York Academy of Sciences. 853 (1): 130–48. Bibcode:1998NYASA.853..130T. doi:10.1111/j.1749-6632.1998.tb08262.x. PMID 10603942. S2CID 86436194.
  13. ^ Wang YX, Zheng YM, Mei QB, Wang QS, Collier ML, Fleischer S, et al. (March 2004). “FKBP12.6 and cADPR regulation of Ca2+ release in smooth muscle cells”. American Journal of Physiology. Cell Physiology. 286 (3): C538-46. doi:10.1152/ajpcell.00106.2003. PMID 14592808. S2CID 20900277.
  14. ^ Tu JC, Xiao B, Yuan JP, Lanahan AA, Leoffert K, Li M, et al. (October 1998). “Homer binds a novel proline-rich motif and links group 1 metabotropic glutamate receptors with IP3 receptors”. Neuron. 21 (4): 717–26. doi:10.1016/S0896-6273(00)80589-9. PMID 9808459. S2CID 2851554.
  15. ^ Chan SL, Mayne M, Holden CP, Geiger JD, Mattson MP (June 2000). “Presenilin-1 mutations increase levels of ryanodine receptors and calcium release in PC12 cells and cortical neurons”. The Journal of Biological Chemistry. 275 (24): 18195–200. doi:10.1074/jbc.M000040200. PMID 10764737.
  16. ^ Gong S, Su BB, Tovar H, Mao C, Gonzalez V, Liu Y, et al. (June 2018). “Polymorphisms Within RYR3 Gene Are Associated With Risk and Age at Onset of Hypertension, Diabetes, and Alzheimer’s Disease”. American Journal of Hypertension. 31 (7): 818–826. doi:10.1093/ajh/hpy046. PMID 29590321.
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External links

Membrane transport protein: ion channels (TC 1A)
Cell signaling: calcium signaling and calcium metabolism

Categories: 

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